Abstract
Three new nicotinamide adenine dinucleotide (NAD) analogs were synthesized, and their characteristics as cofactors for Escherichia coli malic enzyme (ME) and its double mutant ME L310R/Q401C were analyzed. Each pair of the NAD analog and the double mutant showed good orthogonality to the natural pair of NAD and ME in terms of catalyzing oxidative decarboxylation of l-malic acid. Results indicated that molecular interactions between redox enzyme and cofactor could be further explored to generate new bioorthogonal redox systems.
Similar content being viewed by others
References
Belenky P, Bogan KL, Brenner C. NAD(+) metabolism in health and disease. Trends Biochem Sci, 2007, 32(1): 12–19
Ying WH. NAD(+)/NADH and NADP(+)/NADPH in cellular functions and cell death: Regulation and biological consequences. Antioxid Redox Signal, 2008, 10(2): 179–206
Ji DB, Wang L, Hou SH, Liu WJ, Wang JX, Wang Q, Zhao ZK. Creation of bioorthogonal redox systems depending on nicotinamide flucytosine dinucleotide. J Am Chem Soc, 2011, 133(51): 20857–20862
Shah K, Liu Y, Deirmengian C, Shokat KM. Engineering unnatural nucleotide specificity for Rous sarcoma virus tyrosine kinase to uniquely label its direct substrates. Proc Natl Acad Sci USA, 1997, 94(8): 3565–3570
Lin Q, Jiang FY, Schultz PG, Gray NS. Design of allele-specific protein methyltransferase inhibitors. J Am Chem Soc, 2001, 123(47): 11608–11613
Wang R, Zheng W, Yu H, Deng H, Luo M. Labeling substrates of protein arginine methyltransferase with engineered enzymes and matched S-adenosyl-L-methionine analogues. J Am Chem Soc, 2011, 133(20): 7648–7651
Mclachlan MJ, Chockalingam K, Lai KC, Zhao HM. Directed evolution of orthogonal ligand specificity in a single scaffold. Angew Chem Int Ed, 2009, 48(42): 7783–7786
Doyle DF, Braasch DA, Jackson LK, Weiss HE, Boehm MF, Mangelsdorf DJ, Corey DR. Engineering orthogonal ligand-receptor pairs from “near drugs”. J Am Chem Soc, 2001, 123(46): 11367–11371
Hassan AQ, Koh JT. A functionally orthogonal ligand-receptor pair created by targeting the allosteric mechanism of the thyroid hormone receptor. J Am Chem Soc, 2006, 128(27): 8868–8874
Vincent F, Cook SP, Johnson EO, Emmert D, Shah K. Engineering unnatural nucleotide specificity to probe g protein signaling. Chem Biol, 2007, 14(9): 1007–1018
Liu WJ, Wu SG, Hou SH, Zhao ZK. Synthesis of phosphodiester-type nicotinamide adenine dinucleotide analogs. Tetrahedron, 2009, 65(40): 8378–8383
Hou SH, Liu WJ, Ji DB, Wang Q, Zhao ZK. Synthesis of 1,2,3-triazole moiety-containing NAD analogs and their potential as redox cofactors. Tetrahedron Lett, 2011, 52(44): 5855–5857
Hou SH, Liu WJ, Zhao ZK. Synthesis of novel nicotinamide adenine dinucleotide (NAD) analogs and their coenzyme activities. Chin J Org Chem, 2012, 32(2): 349–353
Abramova TV, Vasileva SV, Serpokrylova IY, Kless H, Silnikov VN. A facile and effective synthesis of dinucleotide 5′-triphosphates. Biorg Med Chem, 2007, 15: 6549–6555
Yoshikaw M, Kato T, Takenish T. A novel method for phosphorylation of nucleosides to 5′-nucleotides. Tetrahedron Lett, 1 1967, (50): 5065–5068
Beres J, Bentrude WG, Kruppa G, McKernan PA, Robins RK. Synthesis and antitumor and antiviral activities of a series of 1-beta-D-ribofuranosyl-5-halocytosine (5-halocytidine) cyclic 3′,5′-mono-phosphates. J Med Chem, 1985, 28(4): 418–42
Wang JX, Tan HD, Zhao ZK. Over-expression, purification, and characterization of recombinant NAD-malic enzyme from Escherichia coli K12. Protein Expr Purif, 2007, 53(1): 97–103
Ji DB, Wang L, Zhou YJ, Yang W, Wang Q, Zhao ZK. Oxidative decarboxylation of L-malate by using a synthetic bioredox system. Chin J Catal, 2012, 33(3): 530–535
Author information
Authors and Affiliations
Corresponding author
Rights and permissions
About this article
Cite this article
Ji, D., Wang, L., Liu, W. et al. Synthesis of NAD analogs to develop bioorthogonal redox system. Sci. China Chem. 56, 296–300 (2013). https://doi.org/10.1007/s11426-012-4815-3
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s11426-012-4815-3